We compared the relative amounts and properties of cyclic adenosine 3′:5′-monophosphate (cAMP)-binding proteins in surgical specimens of Wilms' tumor and normal kidney. Cytosolic fractions of both tissues contained type I and type II isozymes of cAMP-dependent protein kinase (adenosine triphosphate: protein phosphotransferase, EC Among tumor samples, the mean ratio of type I to type II cAMP-binding activity was 2.76 ± 0.52 (S.D.) contrasted with 1.36 ± 0.23 for normal kidney (p < 0.001). The total soluble cAMP-binding activities in normal and malignant tissues differed only slightly. Photoaffinity labeling of cytosol from either tissue, using cyclic adenosine 3′:5′-[8-azido-32P]monophosphate, disclosed three cAMP-binding proteins (Mr 47,000, 51,000, and 55,000) that were identified as regulatory subunits of the holoenzyme. Three lower-molecular-weight proteins with unknown function were considered to be proteolytic products of the larger proteins. The Mr 47,000 protein, a monomeric regulatory subunit of type I kinase, was clearly the dominant protein in tumor specimens, but it was much less abundant in normal kidney. The temperature sensitivities of the cAMP-binding proteins and their dissociation constants for cyclic adenosine 3′:5′-[8-azido-32P]monophosphate incorporation did not differ appreciably between tumor and normal tissues. Wilms' tumor appears to have a full complement of regulatory subunits of cAMP-dependent protein kinase that are capable of normal cellular function.


Supported by Childhood Cancer Center Support (Core) Grant CA-21765 and Grant CA-23099 from the National Cancer Institute, by the Ruby Levi Research Fund, and by the American Lebanese Syrian Associated Charities.

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